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Complete amino acid sequence of yeast thioltransferase (glutaredoxin)
Z R Gan1, M A Polokoff, J W Jacobs
1Department of Biological Chemistry, Merck Sharp & Dohme Research Laboratories, West Point, Pennsylvania 19486.
Biochemical and Biophysical Research Communications
|May 16, 1990
Summary
The amino acid sequence of yeast thioltransferase was determined, revealing 106 residues. This yeast enzyme shares structural similarity with pig liver thioltransferase and E. coli glutaredoxin.
Area of Science:
- Biochemistry
- Molecular Biology
- Yeast Genetics
Background:
- Thioltransferase plays a crucial role in cellular redox homeostasis.
- Understanding the structure of thioltransferases from different organisms can elucidate conserved functions.
Purpose of the Study:
- To determine the complete amino acid sequence of thioltransferase from Saccharomyces cerevisiae (yeast).
- To compare the structural features of yeast thioltransferase with homologous proteins from other species.
Main Methods:
- Protein isolation and purification from Saccharomyces cerevisiae.
- Enzymatic and chemical cleavage of thioltransferase into peptides.
- Peptide purification using reverse-phase high-performance liquid chromatography (RP-HPLC).
- Amino acid sequencing via automated Edman degradation.
Main Results:
- The complete amino acid sequence of yeast thioltransferase was elucidated.
- The protein comprises 106 amino acid residues and contains two cysteine residues.
- Significant structural similarity was observed between yeast thioltransferase and pig liver thioltransferase (51%) and E. coli glutaredoxin (34%).
Conclusions:
- The determined sequence provides a basis for understanding the function and evolution of thioltransferases.
- Structural similarities suggest conserved mechanisms of action across different species.
- This research contributes to the field of redox biology and enzyme structure-function relationships.